Targeted engineering of the antibacterial peptide apidaecin, based on an in vivo monitoring assay system

Applied and Environmental Microbiology

Volumn 75, Issue 5, 2009, Pages 1460-1464

  Taguchi, Seiichi ^a   Mita, Kensuke ^a   Ichinohe, Kenta ^a   Hashimoto, Shigeki ^b  

^a HOKKAIDO UNIVERSITY   (Japan)

^b TOKYO UNIVERSITY OF SCIENCE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; AMINO ACID SUBSTITUTIONS; ANTIBACTERIAL PEPTIDES; ASSAY SYSTEMS; DIFFERENTIAL ACTIVITIES; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIUM; IN-VITRO; IN-VIVO; N TERMINALS;

AMINATION; AMINO ACIDS; BACTERIA; ORGANIC ACIDS;

AMINES;

APIDAECIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

AMINO ACID; ANTIBIOTICS; BACTERIUM; BIOASSAY; BIOENGINEERING; MUTATION; PEPTIDE;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; DRUG ACTIVITY; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; IN VIVO STUDY; MINIMUM INHIBITORY CONCENTRATION; MUTAGENESIS; PROMOTER REGION; PROTEIN ENGINEERING; PROTEIN TARGETING; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANTI-BACTERIAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; DIRECTED MOLECULAR EVOLUTION; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION, MISSENSE;

NEGIBACTERIA; POSIBACTERIA;

EID: 61649088165     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02096-08     Document Type: Article

References (26)

1. Bulet, P., C. Hetru, J. L. Dimarcq, and J. A. Hoffmann. 1999. Antimicrobial peptides in insects: structure and function. Dev. Comp. Immunol. 23:329-344.
2. Casteels, P., C. Ampe, F. Jacobs, and P. Tempst. 1993. Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J. Biol. Chem. 268:7044-7054.
3. Casteels, P., C. Ampe, F. Jacobs, C. Vaeck, and P. Tempst. 1989. Apidaecins: antibacterial peptides from honeybees. EMBO J. 8:2387-2391.
4. Casteels, P., J. Romagnolo, M. Castle, K. Casteels-Josson, H. Erdjument-Bromage, and P. Tempst. 1994. Biodiversity of apidaecin-type peptide antibiotics. J. Biol. Chem. 269:26107-26115.
5. Castle, M., A. Nazarian, S. S. Yi, and P. Tempst. 1999. Lethal effects of apidaecin on Escherichia coli involve sequential molecular interactions with diverse targets. J. Biol. Chem. 274:32555-32564.
6. Chopra, I., J. Hodgson, B. Metcalf, and G. Poste. 1997. The search for antimicrobial agents effective against bacteria resistant to multiple antibiotics. Antimicrob. Agents Chemother. 41:497-503.
7. Dutta, R. C., S. Nagpal, and D. M. Salunke. 2008. Functional mapping of apidaecin through secondary structure correlation. Int. J. Biochem. Cell Biol. 40:1005-1015.
8. Fehlbaum, P., P. Bulet, S. Chemysh, J. P. Briand, J. P. Roussel, L. Letellier, C. Hetru, and J. A. Hoffmann. 1996. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog antimicrobial peptides. Proc. Natl. Acad. Sci. USA 6:1221-1225.
9. Futaki, S., T. Suzuki, W. Ohashi, T. Yagami, S. Tanaka, K. Ueda, and Y. Sugiura. 2001. Arginine-rich peptides. An abundant source of membranepermeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276:5836-5840.
10. Gobbo, M., L. Biondi, F. Filira, R. Gennaro, M. Benincasa, B. Scolaro, and R. Rocchi. 2002. Antimicrobial peptides: synthesis and antibacterial activity of linear and cyclic drosocin and apidaecin lb analogues. J. Med. Chem. 45:4494-4504.
11. Hancock, R. E. 1997. Peptide antibiotics. Lancet 349:418-422.
12. Imamura, T., N. Yamamoto, A. Tamura, S. Murabayashi, S. Hashimoto, H. Shimada, and S. Taguchi. 2008. NMR based structure-activity relationship analysis of an antimicrobial peptide, thanatin, engineered by site-specific chemical modification: activity improvement and spectrum alteration. Biochem. Biophys. Res. Commun. 369:609-615.
13. Li, W.-F., G.-X. Ma, and X.-X. Zhou. 2006. Apidaecin-type peptides: biodiversity, structure-function relationships and mode of action. Peptides 27:2350-2359.
14. Otvos, L., Jr., I. O, M. E. Rogers, P. J. Consolvo, B. A. Condie, S. Lovas, P. Bulet, and M. Blaszczyk-Thurin. 2000. Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39:14150-14159.
15. Otvos, L., Jr. 2000. Antibacterial peptides isolated from insects. J. Peptide Sci. 6:497-511.
16. Otvos, L., Jr. 2002. The short proline-rich antibacterial peptide family. Cell. Mol. Life Sci. 59:1138-1150.
17. Otvos, L., Jr., J. D. Wada, F. Lin, B. A. Condie, J. Hanrieder, and R. Hoffmann. 2005. Designer antibacterial peptides kill fluoroquinolone- resistant clinical isolates. J. Med. Chem. 48:5349-5359.
18. Sato, H., and J. B. Feix. 2008. Lysine-enriched cecropin-mellitin antimicrobial peptides with enhanced selectivity. Antimicrob. Agents Chemother. 52:4463-4465.
19. Taguchi, S., I. Kumagai, J. Nakayama, A. Suzuki, and K. Miura. 1989. Efficient extracellular expression of a foreign protein in Streptomyces using secretory protease inhibitor (SSI) gene fusions. Bio/Technology 7:1063-1066.
20. Taguchi, S., K. Kuwasako, A. Suenaga, M. Okada, and H. Momose. 2000. Functional mapping against Escherichia coli for the broad-spectrum antimicrobial peptide, thanatin, based on an in vivo monitoring assay system. J. Biochem. 128:745-754.
21. Taguchi, S., K. Nakagawa, M. Maeno, and H. Momose. 1994. In vivo monitoring system for structure-function relationship analysis of the antibacterial peptide apidaecin. Appl. Environ. Microbiol. 60:3566-3572.
22. Taguchi, S., A. Ozaki, K. Nakagawa, and H. Momose. 1996. Functional mapping of amino acid residues responsible for the antibacterial action of apidaecin. Appl. Environ. Microbiol. 62:4652-4655.
23. Taguchi, S., Y. Yoshida, K. Matsumoto, and H. Momose. 1993. Improved leader and putative terminator sequences for high-level production of Streptomyces subtilisin inhibitor in Escherichia coli. Appl. Microbiol. Biotechnol. 39:732-737.
24. Tomasinsig, L., B. Skerlavaj, N. Papo, B. Giabbai, Y. Shai, and M. Zanetti. 2006. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 281:383-391.
25. Wender, P. A., D. J. Mitchell, K. Pattabiraman, E. T. Pelkey, L. Steinman, and J. B. Rothbard. 2000. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc. Natl. Acad. Sci. USA 97:13003-13008.
26. Zhou, X.-X., W.-F. Li, and Y.-J. Pan. 2008. Functional and structural characterization of apidaecin and its N-terminal and C-terminal fragments. J. Peptide Sci. 14:697-707.